메뉴 건너뛰기




Volumn 44, Issue 16, 2005, Pages 6101-6121

Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: The T-to-THigh quaternary transitions

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CONSTRAINT THEORY; CRYSTALLOGRAPHY; DIMERS; STEREOCHEMISTRY;

EID: 17644375152     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047813a     Document Type: Article
Times cited : (73)

References (66)
  • 1
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • Perutz, M. F. (1989) Mechanisms of cooperativity and allosteric regulation in proteins, Q. Rev. Biophys. 22, 139-237.
    • (1989) Q. Rev. Biophys. , vol.22 , pp. 139-237
    • Perutz, M.F.1
  • 2
    • 0017138398 scopus 로고
    • Oxygenation-linked subunit interactions in human hemoglobin: Experimental studies on the concentration dependence of oxygenation curves
    • Mills, F. C., Johnson, M. L., and Ackers, G. K. (1976) Oxygenation-linked subunit interactions in human hemoglobin: experimental studies on the concentration dependence of oxygenation curves, Biochemistry 15, 5350-5362.
    • (1976) Biochemistry , vol.15 , pp. 5350-5362
    • Mills, F.C.1    Johnson, M.L.2    Ackers, G.K.3
  • 5
    • 0014958178 scopus 로고
    • Inhibition of Bohr effect after removal of C-terminal histidines from haemoglobin β-chains
    • Kilmartin, J. V., and Wootton, J. F. (1970) Inhibition of Bohr effect after removal of C-terminal histidines from haemoglobin β-chains, Nature 228, 766-767.
    • (1970) Nature , vol.228 , pp. 766-767
    • Kilmartin, J.V.1    Wootton, J.F.2
  • 6
    • 0015441684 scopus 로고
    • The effect of removal of C-terminal residues on cooperative interactions in hemoglobin
    • Kilmartin, J. V., and Hewitt, J. A. (1972) The effect of removal of C-terminal residues on cooperative interactions in hemoglobin, Cold Spring Harbor Symp. Quant. Biol. 36, 311-314.
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.36 , pp. 311-314
    • Kilmartin, J.V.1    Hewitt, J.A.2
  • 7
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz, M. F. (1970) Stereochemistry of cooperative effects in haemoglobin, Nature 228, 726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 9
    • 0023022798 scopus 로고
    • Properties of chemically modified Ni(II)-Fe(II) hybrid hemoglobins. Ni-(II) protoporphyrin IX as a model for a permanent deoxy-heme
    • Shibayama, N., Morimoto, H., and Kitagawa, T. (1986) Properties of chemically modified Ni(II)-Fe(II) hybrid hemoglobins. Ni-(II) protoporphyrin IX as a model for a permanent deoxy-heme, J. Mol. Biol. 192, 331-336.
    • (1986) J. Mol. Biol. , vol.192 , pp. 331-336
    • Shibayama, N.1    Morimoto, H.2    Kitagawa, T.3
  • 12
    • 2942715197 scopus 로고    scopus 로고
    • Ligand binding to symmetrical FeZn hybrids of variants of human HbA with modifications in the α1-β2 interface
    • Hui, H. L., Kwiatkowski, L. D., Karasik, E., Colby, J. E., and Noble, R. W. (2004) Ligand binding to symmetrical FeZn hybrids of variants of human HbA with modifications in the α1-β2 interface, Biochemistry 43, 7843-7850.
    • (2004) Biochemistry , vol.43 , pp. 7843-7850
    • Hui, H.L.1    Kwiatkowski, L.D.2    Karasik, E.3    Colby, J.E.4    Noble, R.W.5
  • 13
    • 0032516488 scopus 로고    scopus 로고
    • Structure changes in hemoglobin upon deletion of C-terminal residues, monitored by resonance Raman spectroscopy
    • Wang, D., and Spiro, T. G. (1998) Structure changes in hemoglobin upon deletion of C-terminal residues, monitored by resonance Raman spectroscopy, Biochemistry 37, 9940-9951.
    • (1998) Biochemistry , vol.37 , pp. 9940-9951
    • Wang, D.1    Spiro, T.G.2
  • 14
    • 0035900002 scopus 로고    scopus 로고
    • Mutational effects at the subunit interfaces of human hemoglobin: Evidence for a unique sensitivity of the T quaternary state to changes in the hinge region of the α1β2 interface
    • Noble, R. W., Hui, H. L., Kwiatkowski, L. D., Paily, P., DeYoung, A., Wierzba, A., Colby, J. E., Bruno, S., and Mozzarelli, A. (2001) Mutational effects at the subunit interfaces of human hemoglobin: Evidence for a unique sensitivity of the T quaternary state to changes in the hinge region of the α1β2 interface, Biochemistry 40, 12357-12368.
    • (2001) Biochemistry , vol.40 , pp. 12357-12368
    • Noble, R.W.1    Hui, H.L.2    Kwiatkowski, L.D.3    Paily, P.4    DeYoung, A.5    Wierzba, A.6    Colby, J.E.7    Bruno, S.8    Mozzarelli, A.9
  • 15
    • 0036087535 scopus 로고    scopus 로고
    • Correlation of protein functional properties in the crystal and in solution: The case study of T-state hemoglobin
    • Noble, R. W., Kwiatkowski, A. V., Hui, H. L., Bruno, S., Bettati, S., and Mozzarelli, A. (2002) Correlation of protein functional properties in the crystal and in solution: The case study of T-state hemoglobin, Protein Sci. 11, 1845-1849.
    • (2002) Protein Sci. , vol.11 , pp. 1845-1849
    • Noble, R.W.1    Kwiatkowski, A.V.2    Hui, H.L.3    Bruno, S.4    Bettati, S.5    Mozzarelli, A.6
  • 16
    • 2942717038 scopus 로고    scopus 로고
    • Effects of heterotropic allosteric effectors on the equilibrium and kinetics of the reaction of a single ligand molecule with an α or β subunit of deoxygenated HbA
    • Karasik, E., Kwiatkowski, L. D., Hui, H. L., Colby, J. E., and Noble, R. W. (2004) Effects of heterotropic allosteric effectors on the equilibrium and kinetics of the reaction of a single ligand molecule with an α or β subunit of deoxygenated HbA, Biochemistry 43, 7851-7856.
    • (2004) Biochemistry , vol.43 , pp. 7851-7856
    • Karasik, E.1    Kwiatkowski, L.D.2    Hui, H.L.3    Colby, J.E.4    Noble, R.W.5
  • 17
    • 0035427223 scopus 로고    scopus 로고
    • Allosteric free energy changes at the α1β2 interface of human hemoglobin probed by proton exchange of Trpβ37
    • Mihailescu, M. R., Fronticelli, C., and Russu, I. M. (2001) Allosteric free energy changes at the α1β2 interface of human hemoglobin probed by proton exchange of Trpβ37, Proteins 44, 73-78.
    • (2001) Proteins , vol.44 , pp. 73-78
    • Mihailescu, M.R.1    Fronticelli, C.2    Russu, I.M.3
  • 19
    • 0032584258 scopus 로고    scopus 로고
    • Preparation and kinetic characterization of a series of βW37 variants of human hemoglobin A: Evidence for high-affinity T quaternary structures
    • Kwiatkowski, L. D., Hui, H. L., Wierzba, A., Noble, R. W., Walder, R. Y., Peterson, E. S., Sligar, S. G., and Sanders, K. E. (1998) Preparation and kinetic characterization of a series of βW37 variants of human hemoglobin A: Evidence for high-affinity T quaternary structures, Biochemistry 37, 4325-4335.
    • (1998) Biochemistry , vol.37 , pp. 4325-4335
    • Kwiatkowski, L.D.1    Hui, H.L.2    Wierzba, A.3    Noble, R.W.4    Walder, R.Y.5    Peterson, E.S.6    Sligar, S.G.7    Sanders, K.E.8
  • 20
    • 0032584278 scopus 로고    scopus 로고
    • High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37β: Structural basis for a high-affinity T-state
    • Kavanaugh, J. S., Weydert, J. A., Rogers, P. H., and Arnone, A. (1998) High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37β: Structural basis for a high-affinity T-state, Biochemistry 37, 4358-4373.
    • (1998) Biochemistry , vol.37 , pp. 4358-4373
    • Kavanaugh, J.S.1    Weydert, J.A.2    Rogers, P.H.3    Arnone, A.4
  • 21
    • 0032584325 scopus 로고    scopus 로고
    • A possible allosteric communication pathway identified through a resonance Raman study of four β37 mutants of human hemoglobin A
    • Peterson, E. S., and Friedman, J. M. (1998) A possible allosteric communication pathway identified through a resonance Raman study of four β37 mutants of human hemoglobin A, Biochemistry 37, 4346-4357.
    • (1998) Biochemistry , vol.37 , pp. 4346-4357
    • Peterson, E.S.1    Friedman, J.M.2
  • 22
    • 0346096863 scopus 로고    scopus 로고
    • Crystallographic analysis of the interaction of nitric oxide quaternary-T human hemoglobin
    • Chan, N.-L., Kavanaugh, J. S., Rogers, P. H., and Arnone, A. (2004) Crystallographic analysis of the interaction of nitric oxide quaternary-T human hemoglobin, Biochemistry 43, 118-132.
    • (2004) Biochemistry , vol.43 , pp. 118-132
    • Chan, N.-L.1    Kavanaugh, J.S.2    Rogers, P.H.3    Arnone, A.4
  • 25
    • 0026745130 scopus 로고
    • Functional properties of human hemoglobins synthesized from recombinant mutant β-globins
    • Doyle, M. L., Lew, G., De Young, A., Kwiatkowski, L., Wierzba, A., Noble, R. W., and Ackers, G. K. (1992) Functional properties of human hemoglobins synthesized from recombinant mutant β-globins, Biochemistry 31, 8629-8639.
    • (1992) Biochemistry , vol.31 , pp. 8629-8639
    • Doyle, M.L.1    Lew, G.2    De Young, A.3    Kwiatkowski, L.4    Wierzba, A.5    Noble, R.W.6    Ackers, G.K.7
  • 26
    • 0026760956 scopus 로고
    • High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from β-globins having mutated amino termini
    • Kavanaugh, J. S., Rogers, P. H., and Arnone, A. (1992) High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from β-globins having mutated amino termini, Biochemistry 31, 8640-8647.
    • (1992) Biochemistry , vol.31 , pp. 8640-8647
    • Kavanaugh, J.S.1    Rogers, P.H.2    Arnone, A.3
  • 27
    • 0016824616 scopus 로고
    • Structure of deoxyhemoglobin A crystals grown from polyethylene glycol solutions
    • Ward, K. B., Wishner, B. C., Lattman, E. E., and Love, W. E. (1975) Structure of deoxyhemoglobin A crystals grown from polyethylene glycol solutions, J. Mol. Biol. 98, 161-177.
    • (1975) J. Mol. Biol. , vol.98 , pp. 161-177
    • Ward, K.B.1    Wishner, B.C.2    Lattman, E.E.3    Love, W.E.4
  • 28
    • 0018370503 scopus 로고
    • Investigation of crystalline enzyme-substrate complexes of pyridoxal phosphate-dependent enzymes
    • Metzler, C. M., Rogers, P. H., Arnone, A., Martin, D. S., and Metzler, D. E. (1979) Investigation of crystalline enzyme-substrate complexes of pyridoxal phosphate-dependent enzymes, Methods Enzymol. 62, 551-558.
    • (1979) Methods Enzymol. , vol.62 , pp. 551-558
    • Metzler, C.M.1    Rogers, P.H.2    Arnone, A.3    Martin, D.S.4    Metzler, D.E.5
  • 29
    • 0030000410 scopus 로고    scopus 로고
    • Crystal structure of T state haemoglobin with oxygen bound at all four haems
    • Paoli, M., Liddington, R., Tame, J., Wilkinson, A., and Dodson, G. (1996) Crystal structure of T state haemoglobin with oxygen bound at all four haems, J. Mol. Biol. 256, 775-792.
    • (1996) J. Mol. Biol. , vol.256 , pp. 775-792
    • Paoli, M.1    Liddington, R.2    Tame, J.3    Wilkinson, A.4    Dodson, G.5
  • 30
    • 0014202666 scopus 로고
    • Design of a diffractometer and flow-cell system for x-ray analysis of crystalline proteins with applications to the crystal chemistry of ribonuclease-S
    • Wyckoff, H. W., Doscher, M., Tsernoglou, D., Inagami, T., Johnson, L. N., Hardman, K. D., Allewell, N. M., Kelly, D. M., and Richards, F. M. (1967) Design of a diffractometer and flow-cell system for x-ray analysis of crystalline proteins with applications to the crystal chemistry of ribonuclease-S., J. Mol. Biol. 27, 563-578.
    • (1967) J. Mol. Biol. , vol.27 , pp. 563-578
    • Wyckoff, H.W.1    Doscher, M.2    Tsernoglou, D.3    Inagami, T.4    Johnson, L.N.5    Hardman, K.D.6    Allewell, N.M.7    Kelly, D.M.8    Richards, F.M.9
  • 31
    • 0022326269 scopus 로고
    • Software for a diffractometer with multiwire area detector
    • Howard, A. J., Nielsen, C., and Xuong, N. H. (1985) Software for a diffractometer with multiwire area detector, Methods Enzymol. 114, 452-472.
    • (1985) Methods Enzymol. , vol.114 , pp. 452-472
    • Howard, A.J.1    Nielsen, C.2    Xuong, N.H.3
  • 34
    • 0028103275 scopus 로고
    • Collaborative Computational Project. (1994) Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 35
    • 0026695805 scopus 로고
    • High-resolution x-ray study of deoxyhemoglobin Rothschild 37βTrp→Arg: A mutation that creates an intersubunit chloride-binding site
    • Kavanaugh, J. S., Rogers, P. H., Case, D. A., and Arnone, A. (1992) High-resolution x-ray study of deoxyhemoglobin Rothschild 37βTrp→Arg: a mutation that creates an intersubunit chloride-binding site, Biochemistry 31, 4111-4121.
    • (1992) Biochemistry , vol.31 , pp. 4111-4121
    • Kavanaugh, J.S.1    Rogers, P.H.2    Case, D.A.3    Arnone, A.4
  • 37
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W. A. (1985) Stereochemically restrained refinement of macromolecular structures, Methods Enzymol. 115, 252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 38
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of molecular structures by the maximum-likelihood method
    • Murshudov, G., Vagin, A. A., and Dodson, E. J. (1997) Refinement of molecular structures by the maximum-likelihood method, Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.1    Vagin, A.A.2    Dodson, E.J.3
  • 39
    • 0022333120 scopus 로고
    • Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO
    • Jones, T. A. (1985) Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO, Methods Enzymol. 115, 157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 41
    • 0026597444 scopus 로고
    • Free R-value - A novel statistical quantity for assessing the accuracy of crystal-structures
    • Brünger, A. T. (1992) Free R-value - A novel statistical quantity for assessing the accuracy of crystal-structures, Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 42
    • 0001897686 scopus 로고
    • Assesment of phase accuracy by cross validation: The free R value - Methods and Applications
    • Brünger, A. T. (1993) Assesment of phase accuracy by cross validation: the free R value - Methods and Applications, Acta Crystallogr. D49, 24-36.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 24-36
    • Brünger, A.T.1
  • 43
    • 54749107046 scopus 로고
    • Refinement of a partially oxygenated T state human haemoglobin at 1.5 Å resolution
    • Waller, D. A., and Liddington, R. C. (1990) Refinement of a partially oxygenated T state human haemoglobin at 1.5 Å resolution, Acta Crystallogr. B 46, 409-418.
    • (1990) Acta Crystallogr. B , vol.46 , pp. 409-418
    • Waller, D.A.1    Liddington, R.C.2
  • 44
    • 0016345571 scopus 로고
    • Structure of inositol hexaphosphate-human deoxyhaemoglobin complex
    • Arnone, A., and Perutz, M. F. (1974) Structure of inositol hexaphosphate-human deoxyhaemoglobin complex, Nature 249, 34-36.
    • (1974) Nature , vol.249 , pp. 34-36
    • Arnone, A.1    Perutz, M.F.2
  • 45
    • 0006736046 scopus 로고
    • Mathematical methods used in the comparison of the quaternary structures
    • Cox, J. M. (1967) Mathematical methods used in the comparison of the quaternary structures, J. Mol. Biol. 28, 151-156.
    • (1967) J. Mol. Biol. , vol.28 , pp. 151-156
    • Cox, J.M.1
  • 46
    • 0018361151 scopus 로고
    • Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
    • Baldwin, J., and Chothia, C. (1979) Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism, J. Mol. Biol. 129, 175-220.
    • (1979) J. Mol. Biol. , vol.129 , pp. 175-220
    • Baldwin, J.1    Chothia, C.2
  • 47
    • 0034687668 scopus 로고    scopus 로고
    • Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin
    • Mueser, T. C., Rogers, P. H., and Arnone, A. (2000) Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin, Biochemistry 39, 15353-15364.
    • (2000) Biochemistry , vol.39 , pp. 15353-15364
    • Mueser, T.C.1    Rogers, P.H.2    Arnone, A.3
  • 48
    • 0025777309 scopus 로고
    • Analysis of protein loop closure: Two types of hinges produce one motion in lactate dehydrogenase
    • Gerstein, M., and Chothia, C. (1991) Analysis of protein loop closure: Two types of hinges produce one motion in lactate dehydrogenase, J. Mol. Biol. 220, 133-149.
    • (1991) J. Mol. Biol. , vol.220 , pp. 133-149
    • Gerstein, M.1    Chothia, C.2
  • 50
    • 0031568811 scopus 로고    scopus 로고
    • Structures of a hemoglobin-based blood substitute: Insights into the function of allosteric proteins
    • Kroeger, K. S., and Kundrot, C. E. (1997) Structures of a hemoglobin-based blood substitute: Insights into the function of allosteric proteins, Structure 5, 227-237.
    • (1997) Structure , vol.5 , pp. 227-237
    • Kroeger, K.S.1    Kundrot, C.E.2
  • 51
    • 0014412965 scopus 로고
    • Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: The atomic model
    • Perutz, M. F., Muirhead, H., Cox, J. M., and Goaman, L. C. (1968) Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: the atomic model, Nature 219, 131-139.
    • (1968) Nature , vol.219 , pp. 131-139
    • Perutz, M.F.1    Muirhead, H.2    Cox, J.M.3    Goaman, L.C.4
  • 52
    • 0031586213 scopus 로고    scopus 로고
    • Conformation-invariant structures of the α1β1 human hemoglobin dimer
    • Nichols, W. L., Zimm, B. H., and Ten Eyck, L. F. (1997) Conformation-invariant structures of the α1β1 human hemoglobin dimer, J. Mol. Biol. 270, 598-615.
    • (1997) J. Mol. Biol. , vol.270 , pp. 598-615
    • Nichols, W.L.1    Zimm, B.H.2    Ten Eyck, L.F.3
  • 54
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
    • Perutz, M. F. (1979) Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron, Annu. Rev. Biochem. 48, 327-386.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 56
    • 0001622166 scopus 로고
    • Structure of a dioxygen adduct of (1-methylimidazole)-meso- tetrakis(α,α,α,α-o-pivalamidophenyl)porphinatoiron(II). An iron dioxygen model for the heme component of oxymyoglobin
    • Jameson, G. B., Rodley, G. A., Robinson, W. T., Gagne, R. R., Reed, C. A., and Collman, J. P. (1978) Structure of a dioxygen adduct of (1-methylimidazole)-meso-tetrakis(α,α,α,α-o- pivalamidophenyl)porphinatoiron(II). An iron dioxygen model for the heme component of oxymyoglobin, Inorg. Chem. 17, 850-857.
    • (1978) Inorg. Chem. , vol.17 , pp. 850-857
    • Jameson, G.B.1    Rodley, G.A.2    Robinson, W.T.3    Gagne, R.R.4    Reed, C.A.5    Collman, J.P.6
  • 57
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J.-P. (1965) On the nature of allosteric transitions: a plausible model, J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 58
    • 0021027685 scopus 로고
    • Structure of human oxyhaemoglobin at 2.1 Å resolution
    • Shaanan, B. (1983) Structure of human oxyhaemoglobin at 2.1 Å resolution, J. Mol. Biol. 171, 31-59.
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 59
    • 0021683974 scopus 로고
    • The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution
    • Fermi, G., Perutz, M. F., Shaanan, B., and Fourme, R. (1984) The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution, J. Mol. Biol. 175, 159-174.
    • (1984) J. Mol. Biol. , vol.175 , pp. 159-174
    • Fermi, G.1    Perutz, M.F.2    Shaanan, B.3    Fourme, R.4
  • 60
    • 0025903710 scopus 로고
    • The mutation β99Asp→Tyr stabilizes Y - A new, composite quaternary state of human hemoglobin
    • Smith, F. R., Lattman, E. E., and Carter, C. W. J. (1991) The mutation β99Asp→Tyr stabilizes Y - a new, composite quaternary state of human hemoglobin, Proteins 10, 81-91.
    • (1991) Proteins , vol.10 , pp. 81-91
    • Smith, F.R.1    Lattman, E.E.2    Carter, C.W.J.3
  • 61
    • 0026795182 scopus 로고
    • A third quaternary structure of human hemoglobin A at 1.7-Å resolution
    • Silva, M. M., Rogers, P. H., and Arnone, A. (1992) A third quaternary structure of human hemoglobin A at 1.7-Å resolution, J. Biol. Chem. 267, 17248-17256.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17248-17256
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 63
    • 0028269771 scopus 로고
    • Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary structure
    • Smith, F. R., and Simmons, K. C. (1994) Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary structure, Proteins 18, 295-300.
    • (1994) Proteins , vol.18 , pp. 295-300
    • Smith, F.R.1    Simmons, K.C.2
  • 65
    • 0035006227 scopus 로고    scopus 로고
    • The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 Å resoultion and its relationship to the quaternary structures of other hemoglobin crystal forms
    • Safo, M. K., and Abraham, D. J. (2001) The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 Å resoultion and its relationship to the quaternary structures of other hemoglobin crystal forms, Protein Sci. 10, 1091-1099.
    • (2001) Protein Sci. , vol.10 , pp. 1091-1099
    • Safo, M.K.1    Abraham, D.J.2
  • 66
    • 0005749451 scopus 로고    scopus 로고
    • Structure of human methaemoglobin: The variation of a theme
    • Biswal, B. K., and Vijayan, M. (2001) Structure of human methaemoglobin: The variation of a theme, Curr. Sci. 81, 1100-1105.
    • (2001) Curr. Sci. , vol.81 , pp. 1100-1105
    • Biswal, B.K.1    Vijayan, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.